Localization of cathepsin K in human osteoclasts by in situ hybridization and immunohistochemistry

Littlewood‐Evans, Amanda; Kokubo, Toshio; Ishibashi, Osamu; Inaoka, Tetsuya; Wlodarski, Brenda; Gallagher, James A.; Bilbe, Graeme

doi:10.1016/s8756-3282(96)00351-1

Cited by 182 publications

(99 citation statements)

References 23 publications

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“…However, several studies indicate a predominant expression of cathepsin K in osteoclasts and osteoclast-like giant cells (12,14,15,(31)(32)(33)(34). In the present study, staining of this proteinase was strong in osteoclasts at sites of bone destruction and in multinucleated giant cells of the perimatrix, whereas only few mononuclear cells in this region were detected.…”

Section: Discussioncontrasting

confidence: 52%

Expression of Matrix-Degrading Cysteine Proteinase Cathepsin K in Cholesteatoma

et al. 2001

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Cholesteatoma is a nonneoplastic lesion of the middle ear space or mastoid that is histologically characterized by a progressive bone erosion of the ossicles and surrounding bone. Several matrixdegrading enzymes have been implicated as mediators of this bone erosion. Because the novel cysteine proteinase cathepsin K has been shown to play a central role in bone resorption, we examined the expression of this enzyme in tissue specimens of cholesteatoma. Tissue specimens of 9 patients with cholesteatoma were obtained during middle-ear surgery. Expression of cathepsin K mRNA was determined by RT-PCR using specific primers. Immunohistochemical analysis of cathepsin K protein expression in tissue sections was performed by using the streptavidin-alkaline phosphatase technique. Expression of both cathepsin K mRNA and protein was detected in areas affected by cholesteatoma, whereas specimens of nonaffected ear cartilage and surrounding tissue were not positive. In addition, cathepsin K was detected in numerous multinucleated giant cells, particularly osteoclasts at the site of bone degradation. In contrast, keratinized squamous epithelium was negative for cathepsin K. These data demonstrate that the matrix-degrading cysteine proteinase cathepsin K may be involved in bone erosion in cholesteatoma. Strong expression of this collagenolytic enzyme in osteoclasts suggests that these cells are mainly involved in cathepsin K-mediated bone destruction.

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Section: Discussioncontrasting

confidence: 52%

Expression of Matrix-Degrading Cysteine Proteinase Cathepsin K in Cholesteatoma

et al. 2001

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“…Identification of human osteoclasts cannot be achieved on the basis of a single phenotypic characteristic, but relies on multiparametric approaches based on morphologic (cell size, number of nuclei; 14), cytochemical (TRAP positivity; 15), phenotypic (calcitonin receptor ϩ , vitronectin receptor ϩ , carbonic anhydrase II ϩ ; [16][17][18][19], and functional (bone resorption activity) properties (20). Accordingly, LSC showed that, compared with 121F -cells, 121F…”

Section: Discussionmentioning

confidence: 99%

A new cytometric method for the immunophenotypic characterization of bone‐derived human osteoclasts

et al. 2002

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“…Expression of cathepsin K has been demonstrated in different cell populations like synovial fibroblasts (30), macrophages and smooth muscle cells in atheroma (31), and breast cancer cells (32). However, several studies indicate that cathepsin K is predominantly expressed in osteoclasts (27,33,34). GC sharing phenotypic features of osteoclasts are found within several diseased synovial tissues, as in osteoarthritis (OA), rheumatoid arthritis, pigmented villonodular synovitis, and GCTTS.…”

Section: Discussionmentioning

confidence: 99%

“…As control, mouse immunoglobulins (Cymbus Biotechnology, Chandlers Ford, United Kingdom) were used to replace the primary antibodies. Tissue specimens from a patient with a giant cell tumor of bone were applied as positive control (27). Slides were treated with an avidin/biotin blocking kit (Vector, Burlingame, CA).…”

Section: Immunohistochemistrymentioning

confidence: 99%

Expression of Cysteine Proteinases Cathepsins B and K and of Cysteine Proteinase Inhibitor Cystatin C in Giant Cell Tumor of Tendon Sheath

Hansen

Gäumann

et al. 2001

Modern Pathology

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The expression of cysteine proteinases cathepsins B and K and of the endogenous inhibitor of cysteine proteinases, cystatin C, was investigated in tissue specimens of patients with giant cell tumor of tendon sheath (GCTTS). Expression of both enzymes was examined by immunohistochemistry in tissue specimens of 14 patients with GCTTS. Applying double-labeling techniques, the coexpression of cathepsin B and its major endogenous inhibitor cystatin C was additionally studied. Cells expressing the respective proteins were further characterized with the macrophage markers HAM56 and anti-CD68 (clone PG-M1). Cathepsin B could be detected in numerous HAM56-positive mononuclear cells (MC), but only in very few giant cells (GC). In contrast, cathepsin K was predominantly identified in GC that were also strongly immunoreactive for cystatin C and CD68. Coexpression of cathepsin B and cystatin C occurred only in a few MC. The strong expression of both cathepsin B and K suggests that in GCTTS, bone erosion might be mediated not only by pressure of the proliferative tissue, but also by matrix-degrading cysteine proteinases. Because previous studies showed that osteoclasts express high levels of CD68, cathepsin K, and cystatin C but not of cathepsin B, our study contributes to the view that GC of GCTTS and osteoclasts are closely associated.

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Localization of cathepsin K in human osteoclasts by in situ hybridization and immunohistochemistry

Cited by 182 publications

References 23 publications

Expression of Matrix-Degrading Cysteine Proteinase Cathepsin K in Cholesteatoma

Expression of Matrix-Degrading Cysteine Proteinase Cathepsin K in Cholesteatoma

A new cytometric method for the immunophenotypic characterization of bone‐derived human osteoclasts

Expression of Cysteine Proteinases Cathepsins B and K and of Cysteine Proteinase Inhibitor Cystatin C in Giant Cell Tumor of Tendon Sheath

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